The hydrophobic moment of the amphipathic helix of salmon calcitonin and biological potency
β Scribed by Richard M. EPAND; Jay K. SEYLER; Ronald C. ORLOWSKI
- Book ID
- 115124648
- Publisher
- John Wiley and Sons
- Year
- 1986
- Tongue
- English
- Weight
- 329 KB
- Volume
- 159
- Category
- Article
- ISSN
- 1432-1327
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π SIMILAR VOLUMES
The 32 amino acid hormone human calcitonin was studied at pH 3.7 and 7.4 by multidimensional NMR spectroscopy in sodium dodecyl sulfate micelles at 310K. The secondary structure was obtained from nuclear Overhauser enhancement spectroscopy (NOESY), 3 J HNβ£ coupling constants, and slowly exchanging a
## Abstract The aim of the present investigation is to determine the effect of Ξ±βhelical propensity and sidechain hydrophobicity on the stability of amphipathic Ξ±βhelices. Accordingly, a series of 18βresidue amphipathic Ξ±βhelical peptides has been synthesized as a model system where all 20 amino ac